IN SITU STUDY of GOLD FUNCTIONALIZATION SURFACE for PROTEIN IMMOBILIZATION
Autor(a) principal: | |
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Data de Publicação: | 2014 |
Outros Autores: | , |
Tipo de documento: | Artigo |
Idioma: | por |
Título da fonte: | Repositório Institucional da UNESP |
Texto Completo: | http://dx.doi.org/10.26850/1678-4618EQJ.V39.1.2014.P244-256 http://hdl.handle.net/11449/233723 |
Resumo: | The SAM approach for biological material immobilization is currently used in biosensors devices, for analytical and protein affinity studies. This paper focuses on the study of real time SAM formation consisted of mixed SAM of 11-mercaptoundecanoic acid (MUA) and 6-mercapto-1-hexanol, in a molar ratio of 1:3, on gold surface, by QCM-D and cyclic voltammetry techniques. It was confirmed that the SAM is a packed film, with high degree of surface coverage. As an example of protein adsorption on the SAM, it was studied, by QCM-D technique, the adsorption process of gelatin. The results demonstrate that the adsorption and coverage processes occur in a single step, resulting in the formation of a protein monolayer. This is an interesting result since it partially assures the use of Langmuir isotherm model to study protein affinity and analytical responses. |
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IN SITU STUDY of GOLD FUNCTIONALIZATION SURFACE for PROTEIN IMMOBILIZATIONESTUDO in SITU DA FUNCIONALIZAÇÃO DE SUPERFÍCIE DE OURO PARA IMOBILIZAÇÃO DE PROTEÍNAProtein adsorptionQCM-DSAMThe SAM approach for biological material immobilization is currently used in biosensors devices, for analytical and protein affinity studies. This paper focuses on the study of real time SAM formation consisted of mixed SAM of 11-mercaptoundecanoic acid (MUA) and 6-mercapto-1-hexanol, in a molar ratio of 1:3, on gold surface, by QCM-D and cyclic voltammetry techniques. It was confirmed that the SAM is a packed film, with high degree of surface coverage. As an example of protein adsorption on the SAM, it was studied, by QCM-D technique, the adsorption process of gelatin. The results demonstrate that the adsorption and coverage processes occur in a single step, resulting in the formation of a protein monolayer. This is an interesting result since it partially assures the use of Langmuir isotherm model to study protein affinity and analytical responses.UNESP Instituto de Química, Rua Prof. Francisco Degni n° 55UNESP Instituto de Química, Rua Prof. Francisco Degni n° 55Universidade Estadual Paulista (UNESP)dos Santos, Adriano [UNESP]Ribeiro, Willian Campos [UNESP]Bueno, Paulo Roberto [UNESP]2022-05-01T09:47:25Z2022-05-01T09:47:25Z2014-01-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article244-256http://dx.doi.org/10.26850/1678-4618EQJ.V39.1.2014.P244-256Ecletica Quimica, v. 39, n. 1, p. 244-256, 2014.1678-46180100-4670http://hdl.handle.net/11449/23372310.26850/1678-4618EQJ.V39.1.2014.P244-2562-s2.0-85117593765Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPporEcletica Quimicainfo:eu-repo/semantics/openAccess2022-05-01T09:47:25Zoai:repositorio.unesp.br:11449/233723Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462022-05-01T09:47:25Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
IN SITU STUDY of GOLD FUNCTIONALIZATION SURFACE for PROTEIN IMMOBILIZATION ESTUDO in SITU DA FUNCIONALIZAÇÃO DE SUPERFÍCIE DE OURO PARA IMOBILIZAÇÃO DE PROTEÍNA |
title |
IN SITU STUDY of GOLD FUNCTIONALIZATION SURFACE for PROTEIN IMMOBILIZATION |
spellingShingle |
IN SITU STUDY of GOLD FUNCTIONALIZATION SURFACE for PROTEIN IMMOBILIZATION dos Santos, Adriano [UNESP] Protein adsorption QCM-D SAM |
title_short |
IN SITU STUDY of GOLD FUNCTIONALIZATION SURFACE for PROTEIN IMMOBILIZATION |
title_full |
IN SITU STUDY of GOLD FUNCTIONALIZATION SURFACE for PROTEIN IMMOBILIZATION |
title_fullStr |
IN SITU STUDY of GOLD FUNCTIONALIZATION SURFACE for PROTEIN IMMOBILIZATION |
title_full_unstemmed |
IN SITU STUDY of GOLD FUNCTIONALIZATION SURFACE for PROTEIN IMMOBILIZATION |
title_sort |
IN SITU STUDY of GOLD FUNCTIONALIZATION SURFACE for PROTEIN IMMOBILIZATION |
author |
dos Santos, Adriano [UNESP] |
author_facet |
dos Santos, Adriano [UNESP] Ribeiro, Willian Campos [UNESP] Bueno, Paulo Roberto [UNESP] |
author_role |
author |
author2 |
Ribeiro, Willian Campos [UNESP] Bueno, Paulo Roberto [UNESP] |
author2_role |
author author |
dc.contributor.none.fl_str_mv |
Universidade Estadual Paulista (UNESP) |
dc.contributor.author.fl_str_mv |
dos Santos, Adriano [UNESP] Ribeiro, Willian Campos [UNESP] Bueno, Paulo Roberto [UNESP] |
dc.subject.por.fl_str_mv |
Protein adsorption QCM-D SAM |
topic |
Protein adsorption QCM-D SAM |
description |
The SAM approach for biological material immobilization is currently used in biosensors devices, for analytical and protein affinity studies. This paper focuses on the study of real time SAM formation consisted of mixed SAM of 11-mercaptoundecanoic acid (MUA) and 6-mercapto-1-hexanol, in a molar ratio of 1:3, on gold surface, by QCM-D and cyclic voltammetry techniques. It was confirmed that the SAM is a packed film, with high degree of surface coverage. As an example of protein adsorption on the SAM, it was studied, by QCM-D technique, the adsorption process of gelatin. The results demonstrate that the adsorption and coverage processes occur in a single step, resulting in the formation of a protein monolayer. This is an interesting result since it partially assures the use of Langmuir isotherm model to study protein affinity and analytical responses. |
publishDate |
2014 |
dc.date.none.fl_str_mv |
2014-01-01 2022-05-01T09:47:25Z 2022-05-01T09:47:25Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://dx.doi.org/10.26850/1678-4618EQJ.V39.1.2014.P244-256 Ecletica Quimica, v. 39, n. 1, p. 244-256, 2014. 1678-4618 0100-4670 http://hdl.handle.net/11449/233723 10.26850/1678-4618EQJ.V39.1.2014.P244-256 2-s2.0-85117593765 |
url |
http://dx.doi.org/10.26850/1678-4618EQJ.V39.1.2014.P244-256 http://hdl.handle.net/11449/233723 |
identifier_str_mv |
Ecletica Quimica, v. 39, n. 1, p. 244-256, 2014. 1678-4618 0100-4670 10.26850/1678-4618EQJ.V39.1.2014.P244-256 2-s2.0-85117593765 |
dc.language.iso.fl_str_mv |
por |
language |
por |
dc.relation.none.fl_str_mv |
Ecletica Quimica |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
244-256 |
dc.source.none.fl_str_mv |
Scopus reponame:Repositório Institucional da UNESP instname:Universidade Estadual Paulista (UNESP) instacron:UNESP |
instname_str |
Universidade Estadual Paulista (UNESP) |
instacron_str |
UNESP |
institution |
UNESP |
reponame_str |
Repositório Institucional da UNESP |
collection |
Repositório Institucional da UNESP |
repository.name.fl_str_mv |
Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP) |
repository.mail.fl_str_mv |
|
_version_ |
1799964575467044864 |